dbPTM

NTF2_SCHPO - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NTF2_SCHPO
UniProt AC	Q10100
Protein Name	Nuclear transport factor 2
Gene Name	ntf2
Organism	Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length	123
Subcellular Localization	Cytoplasm.
Protein Description	Facilitates protein transport into the nucleus. Could be part of a multicomponent system of cytosolic factors that assemble at the pore complex during nuclear import (By similarity)..
Protein Sequence	MADYNALATQFTQFYYQTFDSDRSQLSSLYREESMLSFEGAQLQGTKAIVEKLVSLPFQRVQHRISTLDAQPTGTTGSVIVMVTGELLLDEEQMAQRYSQVFHLVNNNGNYYVLNDLFRLNYG

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference	Orthologous Protein Cluster
Oops, there are no PTM records of NTF2_SCHPO !!

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
Oops, there are no upstream regulatory protein records of NTF2_SCHPO !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of NTF2_SCHPO !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of NTF2_SCHPO !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of NTF2_SCHPO !!

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of NTF2_SCHPO

Related Literatures of Post-Translational Modification